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06-735

Sigma-Aldrich

Anti-Caspase 3 Antibody

Upstate®, from rabbit

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Synonym(s):
Anti-CASP-3, Anti-Caspase-3
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

species reactivity

mouse, human, rat

manufacturer/tradename

Upstate®

technique(s)

immunohistochemistry: suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... CASP3(836)

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ABC495AB187106-503-I
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06-735

Anti-Caspase 3 Antibody

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ABC495

Anti-Caspase 3 Antibody

vibrant-m

AB1871

Anti-Caspase 1 Antibody

vibrant-m

06-503-I

Anti-Caspase 1 Antibody

species reactivity

mouse, human, rat

species reactivity

human, mouse

species reactivity

human, rat, mouse

species reactivity

human

antibody form

purified immunoglobulin

antibody form

affinity isolated antibody

antibody form

affinity purified immunoglobulin

antibody form

affinity isolated antibody

biological source

rabbit

biological source

rabbit

biological source

rabbit

biological source

rabbit

NCBI accession no.

NM_032991

NCBI accession no.

NP_004337

NCBI accession no.

NM_001223.3, NM_033292.2, NM_033293.2, NM_033294.2, NM_033295.2

NCBI accession no.

NP_001214

technique(s)

immunohistochemistry: suitable, western blot: suitable

technique(s)

immunocytochemistry: suitable, western blot: suitable

technique(s)

immunofluorescence: suitable, immunoprecipitation (IP): suitable, western blot: suitable

technique(s)

immunohistochemistry: suitable (paraffin), western blot: suitable

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General description

Caspase-3 (UniProt: P42574; also known as EC:3.4.22.56, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1) is encoded by the CASP3 (also known as CPP32) gene (Gene ID: 836) in human. Cysteine-aspartic proteases or Caspases play essential roles in apoptosis, necrosis, and inflammation. Historically, caspases were numbered in the order in which they were identified. Caspase-3 is a heterotetrameric enzyme that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. Caspase-3 is initially produced with a propeptide sequence (aa 1-9), the removal of which yields the 268 aa. caspase-3 proenzyme. Upon activation, the proenzyme is proteolytically cleaved first between Asp175-Ser176 to generate a p20 (aa 10-175) fragment and the p12 (aa 176-277) subunit. Further cleavage of the p20 fragment between Asp28-Ser29 produces the p17 (aa 29-175) subunit. The p17 and p12 subunits dimerize and forms the active caspase-3 enzyme. Caspase-3 has a strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position. Caspase-3 is involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a Asp216-|-Gly217 bond. Caspase-3 mediates the proteolytic activation of caspases-6 and -7, while caspase-3 itself is processed and activated by caspase-8, -9, or -10.

Specificity

Recognizes full-length Caspase 3 (Yama/Apopain) and proteolytic fragments.

Immunogen

Human full-length Caspase 3 fusion protein containing a histidine-6 tag

application

This Anti-Caspase 3 Antibody is validated for use in Immunihistochmistry and Western Blotting for the detection of Caspase 3.
Western Blotting Analysis: 1μg/mL of this antibody detects Caspase-3 in A431 cell lysate.

Immunohistochemistry (Paraffin) Analysis: A 1:250 dilution of this antibody detected Caspase-3 in Human tonsil tissue sections.

Quality

routinely evaluated by immunoblot on RIPA lysates from non-stimulated human A431 cells, mouse 3T3/A31 or rat PC12 cells

Target description

32 kDa

Linkage

Replaces: 04-1090; 04-439

Physical form

Format: Purified
Protein A purified IgG in of 0.1M Tris-glycine, pH 7.4, 0.15M NaCl,and 0.05% sodium azide.

Storage and Stability

Stable for 2 years at 2-8°C from date of shipment. For maximum recovery of product, centrifuge the original vial prior to removing the cap.

Analysis Note

Control
Positive Antigen Control: Catalog #12-301, non-stimulated A431 cell lysate. Add 2.5µL of 2-mercaptoethanol/100µL of lysate and boil for 5 minutes to reduce the preparation. Load 20µg of reduced lysate per lane for mingels.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1


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Antiandrogen-induced cell death in LNCaP human prostate cancer cells.
Lee, EC; Zhan, P; Schallhom, R; Packman, K; Tenniswood, M
Cell Death and Differentiation null
Prisca Boisguérin et al.
Cardiovascular research, 116(3), 633-644 (2019-05-31)
Regulated cell death is a main contributor of myocardial ischaemia-reperfusion (IR) injury during acute myocardial infarction. In this context, targeting apoptosis could be a potent therapeutical strategy. In a previous study, we showed that DAXX (death-associated protein) was essential for
A caspase cascade regulating developmental axon degeneration.
Simon, DJ; Weimer, RM; McLaughlin, T; Kallop, D; Stanger, K; Yang, J; O'Leary et al.
The Journal of Neuroscience null
M Leist et al.
Biochemical and biophysical research communications, 258(1), 215-221 (1999-05-01)
The endogenous mediator nitric oxide (NO) blocked apoptosis of Jurkat cells elicited by staurosporine, anti-CD95 or chemotherapeutics, and switched death to necrosis. The switch in the mode of cell death was dependent on the ATP loss elicited by NO. This
Ying Wang et al.
Neuroreport, 23(18), 1052-1058 (2012-11-01)
Necrosis and apoptosis are well established as two primary cell death pathways. Mixed neuroglial cultures are commonly used to study cell death mechanisms in neural cells. However, the ages of these cultures vary across studies and little attention has been

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